The chaperonin GroEL of the heat shock protein family from Escherichia coli cells can bind various polypeptides lacking rigid tertiary structure and thus prevent their nonspecific association and provide for acquisition of native conformation. In the present work we studied the interaction of GroEL with six denatured proteins (α-lactalbumin, ribonuclease A, egg lysozyme in the presence of dithiothreitol, pepsin, β-casein, and apocytochrome c) possessing negative or positive total charge at… CONTINUE READING